Interaction of herpes simplex virus 1 origin-binding protein with DNA polymerase α

Sam S.K. Lee, Qun Dong, T. S.F. Wang, I. R. Lehman

Research output: Contribution to journalArticlepeer-review

25 Scopus citations

Abstract

The herpes simplex virus 1 (HSV-1) genome encodes seven polypeptides that are required for its replication. These include a heterodimeric DNA polymerase, a single-strand-DNA-binding protein, a heterotrimeric helicase/primase, and a protein (UL9 protein) that hinds specifically to an HSV-1 origin of replication (ori(s)). We demonstrate here that UL9 protein interacts specifically with the 180-kDa catalytic subunit of the cellular DNA polymerase α-primase. This interaction can be detected by immunoprecipitation with antibodies directed against either of these proteins, by gel mobility shift of an ori(s)-UL9 protein complex, and by stimulation of DNA polymerase activity by the UL9 protein. These findings suggest thai enzymes required for cellular DNA replication also participate in HSV-1 DNA replication.

Original languageEnglish (US)
Pages (from-to)7882-7886
Number of pages5
JournalProceedings of the National Academy of Sciences of the United States of America
Volume92
Issue number17
DOIs
StatePublished - Aug 15 1995

Keywords

  • DNA replication
  • UL9 protein
  • protein-protein interactions

ASJC Scopus subject areas

  • General

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